LIN2_LOTJA
ID LIN2_LOTJA Reviewed; 1485 AA.
AC D1FP57; D1FP58;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Putative E3 ubiquitin-protein ligase LIN-2 {ECO:0000303|PubMed:19776163};
DE Short=LjLIN {ECO:0000303|PubMed:19776163};
DE EC=2.3.2.27 {ECO:0000303|PubMed:19776163};
DE AltName: Full=RING-type E3 ubiquitin transferase LIN-2 {ECO:0000305};
GN Name=LIN {ECO:0000312|EMBL:ACL14423.1};
OS Lotus japonicus (Lotus corniculatus var. japonicus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus.
OX NCBI_TaxID=34305;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ACL14423.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF ASP-1267.
RX PubMed=19776163; DOI=10.1104/pp.109.143933;
RA Kiss E., Olah B., Kalo P., Morales M., Heckmann A.B., Borbola A., Lozsa A.,
RA Kontar K., Middleton P., Downie J.A., Oldroyd G.E., Endre G.;
RT "LIN, a novel type of U-box/WD40 protein, controls early infection by
RT rhizobia in legumes.";
RL Plant Physiol. 151:1239-1249(2009).
CC -!- FUNCTION: Putative E3 ubiquitin-protein ligase involved in the
CC rhizobial infection process. Plays an important role in the early steps
CC of infection thread formation and in growth and differentiation of
CC nodules. {ECO:0000269|PubMed:19776163}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000303|PubMed:19776163};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000303|PubMed:19776163}.
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DR EMBL; EU926664; ACL14423.1; -; mRNA.
DR EMBL; EU926665; ACL14424.1; -; mRNA.
DR AlphaFoldDB; D1FP57; -.
DR SMR; D1FP57; -.
DR UniPathway; UPA00143; -.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0009877; P:nodulation; IEA:UniProtKB-KW.
DR CDD; cd16664; RING-Ubox_PUB; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045210; RING-Ubox_PUB.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00504; Ubox; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS51698; U_BOX; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Nodulation; Repeat; Transferase; WD repeat.
FT CHAIN 1..1485
FT /note="Putative E3 ubiquitin-protein ligase LIN-2"
FT /id="PRO_0000413000"
FT DOMAIN 510..585
FT /note="U-box"
FT REPEAT 1194..1232
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 1246..1283
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 1409..1448
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 1454..1485
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REGION 337..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..351
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 1267
FT /note="D->N: In Ljsym7; impaired nodulation and rhizobial
FT infection."
FT /evidence="ECO:0000269|PubMed:19776163"
SQ SEQUENCE 1485 AA; 166327 MW; 1D7ECC0E894214FF CRC64;
MAGNFRFMMD QKDIVRFLTT TVDSFIQDRL INKEQRTQHK EQCAERLAAE DGSGDKDTEV
EYSDQAVLAN LDWGIEALEE AINTYNMETK LARLDYAEKM LQVCAMLNPK QKIAGVPNSY
LSAWAHLNLS YLWKLRNNVQ NCISHALEMF IVDPFFTRID FAPELWKSLF LPHMSSIVGW
YSEERHRLMM EVIPDSADLS FTADFEQFFN ESLVLTMRPH QLEKLQKLEQ LYGESLDENT
KLYAKYYNDC MNSDSSSSKK AVPMLPIAEP PMTPLHELSR TIPDFVKFGP ILPKSAGFSL
APRSKDVLNE TIRENVTSSN LKEEKLSIWG AKDTIIEENE DDSDSELDNE SVDSDDKNNI
FSPGMKMMKY EGVETKVDLS CQRNQIPSPD IFSPLDSPRT APNNSSPNPD MHSKRDSKFL
RLSSSRIREP TISDSLTSSP DISIDNISNA DNEVMVRNNI KRKNDSQTPS MNQDNENSLV
LNDSSHCESE DGYQSSSSLP KLEKLSMGSK PPKDFVCPIT GQIFCDPVTL ETGQTYERKA
IQEWLRTGNT TCPITRQPLS ASILPKTNYV LKRLITSWKE QNPELAQEFS NVNTPRGSSC
SPSAKDIPML STRQRTTDSP NHKNKDYARQ RSNRFMPAAI TTSPTSVLSQ AAVETIVNSL
KPYISSLCTS ENLPECEEAV LKIARLLKDS KTNPQIHSYL SKPTIINGLV EILSASRNRE
VLRTSIYILS ELIFTDDSVA ETLNSVDSDF DCLATLLKNG LAEAALLIYQ LRPVFAQLSA
HELIPSLVDV IQNKNEELDD FQLVIDPKDA AIAILEQTLM GGDEYSRSLN ASSVISANGI
PTLVKYLERM EGRRSVVSVL LCCMQAEKSC KNLIANRIEL SPVLELFHSG NDSVRGTCVE
FLSELVQLNR RTSCNQLLHT IKDEGAFSTM HTFLVYLQMA PMEHQLAVAS LLLQLDLLAE
PRKMSIYREE AVETLIEALW QKDFSNTQMK ALDALLFLIG HISSSGKSYT EAWLLKIAGF
DQPYNALMKV EQLGQHDNDL IETMEDEKNA LNSWQKRIAS VLCNHENGSI FKALEECLKS
NSLKMAKSCL VLATWLTRML YTLPDTGVRD VARKSLLEEV IKVLHSSKSL EDMILVTLSL
YPFISDPTVH EVLRVYAKSI YRILRKLKKY STVAADILKA LLNLNSVDVT ELWSCKEVVE
LDLSSNGEVL SLHYLNGQVL SGLMDGTSKV CDARKRIPRV IQETHEHTKA VTSLCSSGDR
LYSASLDKTI RVWTIKSDGI KCIDVYDIKE AVHELAANDK LACYVSQGTG VKVFNWSEAP
KLINFSKYVK SLAVAGDKLY CGCSGYSIQE VDLSTYTSNS FFTGTRKLLG KQTIHSLQIH
DDYLFACVSS VDATAGKIFS LSQKMVVGSL STGLDIHRIA INSDFIFAGT KFGTIEVWLK
DKFTRVASIQ MAGGHTKITS LVSDVDGMML FVGSSDGKIQ VWALD
